7v5l: Difference between revisions

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<StructureSection load='7v5l' size='340' side='right'caption='[[7v5l]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
<StructureSection load='7v5l' size='340' side='right'caption='[[7v5l]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7v5l]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7V5L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V5L FirstGlance]. <br>
<table><tr><td colspan='2'>[[7v5l]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7V5L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V5L FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Bleomycin_hydrolase Bleomycin hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.40 3.4.22.40] </span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.74&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7v5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v5l OCA], [https://pdbe.org/7v5l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v5l RCSB], [https://www.ebi.ac.uk/pdbsum/7v5l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v5l ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7v5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v5l OCA], [https://pdbe.org/7v5l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v5l RCSB], [https://www.ebi.ac.uk/pdbsum/7v5l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v5l ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/BLMH_HUMAN BLMH_HUMAN]] The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B-aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity (By similarity).  
[https://www.uniprot.org/uniprot/BLMH_HUMAN BLMH_HUMAN] The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B-aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human bleomycin hydrolase (hBH) catalyzes deamidation of the anticancer drug bleomycins (BLM). This enzyme is involved in BLM detoxification and drug resistance. Herein, we report the putative BLM-binding site and catalytic mechanism of hBH. The crystal structures and biochemical studies suggest that hBH cleaves its C-terminal residue without significant preference for the type of amino acid, and therefore can accordingly accommodate the beta-aminoalanine amide moiety of BLM for deamidation. Interestingly, hBH is capable of switching from a cysteine protease to a serine protease that is unable to cleave the secondary amide of hBH C-terminus but reacts with the primary amide of BLMs.
 
The Structure-Function Relationship of Human Bleomycin Hydrolase: Mutation of a Cysteine Protease into a Serine Protease.,Zheng YZ, Cui J, Wang YL, Huang SJ, Lin EC, Huang SC, Rudolf JD, Yan X, Chang CY Chembiochem. 2022 Jun 20;23(12):e202200186. doi: 10.1002/cbic.202200186. Epub, 2022 May 5. PMID:35467071<ref>PMID:35467071</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7v5l" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bleomycin hydrolase]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chang, C Y]]
[[Category: Chang CY]]
[[Category: Huang, S J]]
[[Category: Huang SJ]]
[[Category: Lin, E C]]
[[Category: Lin EC]]
[[Category: Toh, S I]]
[[Category: Toh SI]]
[[Category: Wang, Y L]]
[[Category: Wang YL]]
[[Category: Zheng, Y Z]]
[[Category: Zheng YZ]]
[[Category: Cysteine protease]]
[[Category: Hydrolase]]

Latest revision as of 20:20, 29 November 2023

Crystal structure of human bleomycin hydrolaseCrystal structure of human bleomycin hydrolase

Structural highlights

7v5l is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.74Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BLMH_HUMAN The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B-aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity (By similarity).

7v5l, resolution 1.74Å

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